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Article

14-3-3 binding to LRRK2 is disrupted by multiple Parkinson's disease-associated mutations and regulates cytoplasmic localization.

The Biochemical journal - 15 Sept 2010

Nichols R Jeremy, Dzamko Nicolas, Morrice Nicholas A, Campbell David G, Deak Maria, Ordureau Alban, Macartney Thomas, Tong Youren, Shen Jie, Prescott Alan R, Alessi Dario R

Abstract excerpt

LRRK2 (leucine-rich repeat protein kinase 2) is mutated in a significant number of Parkinson's disease patients, but still little is understood about how it is regulated or functions. In the present study we have demonstrated that 14-3-3 protein isoforms interact with LRRK2. Consistent with this, endogenous LRRK2 isolated from Swiss 3T3 cells or various mouse tissues is associated with endogenous 14-3-3 isoforms....

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Identifiers

PMID: 20642453
DOI: 10.1042/BJ20100483
PMCID: PMC2932554

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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14-3-3 binding to LRRK2 is disrupted by multiple Parkinson's disease-associated mutations and regulates cytoplasmic localization.PMID 20642453Read ↗

Inhibition of LRRK2 kinase activity leads to dephosphorylation of Ser(910)/Ser(935), disruption of 14-3-3 binding and altered cytoplasmic localization.Semantic proximity Read ↗

Phosphorylation-dependent 14-3-3 binding to LRRK2 is impaired by common mutations of familial Parkinson's disease.Semantic proximity Read ↗

14-3-3 phosphorylation inhibits 14-3-3θ's ability to regulate LRRK2 kinase activity and toxicity.Semantic proximity Read ↗

14-3-3 phosphorylation inhibits 14-3-3θ’s ability to regulate LRRK2 kinase activitySemantic proximity Read ↗

Binding of the Human 14-3-3 Isoforms to Distinct Sites in the Leucine-Rich Repeat Kinase 2Semantic proximity Read ↗

14-3-3 binding maintains the Parkinson's associated kinase LRRK2 in an inactive state.Semantic proximity Read ↗

14-3-3 binding maintains the Parkinson’s associated kinase LRRK2 in an inactive stateSemantic proximity Read ↗

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Divergent Effects of G2019S and R1441C LRRK2 Mutations on LRRK2 and Rab10 Phosphorylations in Mouse Tissues.Semantic proximity Read ↗

14-3-3 Proteins regulate mutant LRRK2 kinase activity and neurite shortening.Semantic proximity Read ↗

LRRK2 Phosphorylation: Behind the Scenes.Semantic proximity Read ↗

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